A0A8S0HA38 · A0A8S0HA38_9PSED
- ProteinChaperone SurA
- GenesurA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids440 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation.
Catalytic activity
- [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | outer membrane-bounded periplasmic space | |
Molecular Function | peptide binding | |
Molecular Function | peptidyl-prolyl cis-trans isomerase activity | |
Molecular Function | unfolded protein binding | |
Biological Process | Gram-negative-bacterium-type cell outer membrane assembly | |
Biological Process | protein folding | |
Biological Process | protein stabilization |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameChaperone SurA
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionA0A8S0HA38
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Is capable of associating with the outer membrane.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-27 | |||||
Sequence: MNVKTKLSDCLRPLMLGALFLSTAASA | ||||||
Chain | PRO_5035979343 | 28-440 | Chaperone SurA | |||
Sequence: AVQSIDKVVAIVDNDVVMQSQLDQRVHEVQQTIAKRGGGVPPTSVLEQQVLERLIVENLQLQIGERSGIRITDEELNQAIGTIAQRNSMSIEQFRAALAHDGLSYEDARDQVRREMIISRVRQRRVAERIQVSEQEVKNFLASDLGKMQLSEELHLANILIPTPESANSEAIQSAARQAMEVYQQLKQGADFAQLAIARSGSDNALEGGDMGWRKAAQLPPPFDRELSAMAVGDITQPARTPGGFIILKLLDKRGGGNQVRDEVHVRHILIKPSEIRSEEETKRLAQKLYDRIEAGEDFAELAKNYSEDPGSALNGGDLNWIDPNALVPEFREVMAKTPQGQLSKPFKSPYGWHVLEVLGRRATDSTSQAREQQAMTVLRNRKYDEELQTWLRQIRDEAYVEIKLPGAEQAAQ |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 178-279 | PpiC | ||||
Sequence: SEELHLANILIPTPESANSEAIQSAARQAMEVYQQLKQGADFAQLAIARSGSDNALEGGDMGWRKAAQLPPPFDRELSAMAVGDITQPARTPGGFIILKLLD | ||||||
Domain | 288-387 | PpiC | ||||
Sequence: RDEVHVRHILIKPSEIRSEEETKRLAQKLYDRIEAGEDFAELAKNYSEDPGSALNGGDLNWIDPNALVPEFREVMAKTPQGQLSKPFKSPYGWHVLEVLG |
Domain
The PPIase activity resides only in the second parvulin domain. The N-terminal region and the C-terminal tail are necessary and sufficient for the chaperone activity of SurA. The PPIase activity is dispensable for SurA to function as a chaperone. The N-terminal region and the C-terminal tail are also required for porin recognition.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length440
- Mass (Da)49,032
- Last updated2022-10-12 v1
- Checksum5D564C3AF98B504D
Keywords
- Technical term